1nhy
From Proteopedia
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- | [[Image:1nhy.jpg|left|200px]] | + | [[Image:1nhy.jpg|left|200px]] |
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- | '''Crystal Structure of the GST-like Domain of Elongation Factor 1-gamma from Saccharomyces cerevisiae.''' | + | {{Structure |
+ | |PDB= 1nhy |SIZE=350|CAPTION= <scene name='initialview01'>1nhy</scene>, resolution 3.0Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= TEF3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | ||
+ | }} | ||
+ | |||
+ | '''Crystal Structure of the GST-like Domain of Elongation Factor 1-gamma from Saccharomyces cerevisiae.''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1NHY is a [ | + | 1NHY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NHY OCA]. |
==Reference== | ==Reference== | ||
- | The crystal structure of the glutathione S-transferase-like domain of elongation factor 1Bgamma from Saccharomyces cerevisiae., Jeppesen MG, Ortiz P, Shepard W, Kinzy TG, Nyborg J, Andersen GR, J Biol Chem. 2003 Nov 21;278(47):47190-8. Epub 2003 Sep 12. PMID:[http:// | + | The crystal structure of the glutathione S-transferase-like domain of elongation factor 1Bgamma from Saccharomyces cerevisiae., Jeppesen MG, Ortiz P, Shepard W, Kinzy TG, Nyborg J, Andersen GR, J Biol Chem. 2003 Nov 21;278(47):47190-8. Epub 2003 Sep 12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12972429 12972429] |
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: protein synthesis]] | [[Category: protein synthesis]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:57:08 2008'' |
Revision as of 10:57, 20 March 2008
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, resolution 3.0Å | |||||||
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Ligands: | |||||||
Gene: | TEF3 (Saccharomyces cerevisiae) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Crystal Structure of the GST-like Domain of Elongation Factor 1-gamma from Saccharomyces cerevisiae.
Overview
The crystal structure of the N-terminal 219 residues (domain 1) of the conserved eukaryotic translation elongation factor 1Bgamma (eEF1Bgamma), encoded by the TEF3 gene in Saccharomyces cerevisiae, has been determined at 3.0 A resolution by the single wavelength anomalous dispersion technique. The structure is overall very similar to the glutathione S-transferase proteins and contains a pocket with architecture highly homologous to what is observed in glutathione S-transferase enzymes. The TEF3-encoded form of eEF1Bgamma has no obvious catalytic residue. However, the second form of eEF1Bgamma encoded by the TEF4 gene contains serine 11, which may act catalytically. Based on the x-ray structure and gel filtration studies, we suggest that the yeast eEF1 complex is organized as an [eEF1A.eEF1Balpha.eEF1Bgamma]2 complex. A 23-residue sequence in the middle of eEF1Bgamma is essential for the stable dimerization of eEF1Bgamma and the quaternary structure of the eEF1 complex.
About this Structure
1NHY is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
The crystal structure of the glutathione S-transferase-like domain of elongation factor 1Bgamma from Saccharomyces cerevisiae., Jeppesen MG, Ortiz P, Shepard W, Kinzy TG, Nyborg J, Andersen GR, J Biol Chem. 2003 Nov 21;278(47):47190-8. Epub 2003 Sep 12. PMID:12972429
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